JAG1B_DANRE
ID JAG1B_DANRE Reviewed; 1213 AA.
AC Q90Y54;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein jagged-1b;
DE Short=Jagged1b;
DE AltName: Full=Jagged3;
DE Flags: Precursor;
GN Name=jag1b; Synonyms=jag3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oda T., Chandrasekharappa S.C.;
RT "Isolation, characterization and expression analysis of zebrafish Jagged
RT genes.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ligand for Notch receptors and involved in the mediation of
CC Notch signaling (By similarity). Seems to be involved in cell-fate
CC decisions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:P78504}.
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DR EMBL; AF229451; AAL08216.1; -; mRNA.
DR AlphaFoldDB; Q90Y54; -.
DR SMR; Q90Y54; -.
DR STRING; 7955.ENSDARP00000008197; -.
DR PaxDb; Q90Y54; -.
DR PRIDE; Q90Y54; -.
DR ZFIN; ZDB-GENE-011128-4; jag1b.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q90Y54; -.
DR PhylomeDB; Q90Y54; -.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR SignaLink; Q90Y54; -.
DR PRO; PR:Q90Y54; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; NAS:ZFIN.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0060117; P:auditory receptor cell development; IMP:ZFIN.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:ZFIN.
DR GO; GO:1904888; P:cranial skeletal system development; IMP:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0031017; P:exocrine pancreas development; IGI:ZFIN.
DR GO; GO:0060325; P:face morphogenesis; IMP:ZFIN.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:ZFIN.
DR GO; GO:0035622; P:intrahepatic bile duct development; IGI:ZFIN.
DR GO; GO:0001889; P:liver development; IGI:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0032474; P:otolith morphogenesis; IMP:ZFIN.
DR GO; GO:0031016; P:pancreas development; IGI:ZFIN.
DR GO; GO:0060872; P:semicircular canal development; IMP:ZFIN.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IMP:ZFIN.
DR GO; GO:0030878; P:thyroid gland development; IMP:ZFIN.
DR InterPro; IPR001774; DSL.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR033108; Jag1.
DR InterPro; IPR026219; Jagged/Serrate.
DR InterPro; IPR011651; Notch_ligand_N.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR24049:SF18; PTHR24049:SF18; 2.
DR Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF07657; MNNL; 1.
DR PRINTS; PR02059; JAGGEDFAMILY.
DR SMART; SM00051; DSL; 1.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00214; VWC; 1.
DR SMART; SM00215; VWC_out; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS51051; DSL; 1.
DR PROSITE; PS00022; EGF_1; 16.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 8.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1213
FT /note="Protein jagged-1b"
FT /id="PRO_0000007631"
FT TOPO_DOM 27..1064
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1065..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..226
FT /note="DSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT DOMAIN 227..260
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 261..291
FT /note="EGF-like 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 293..331
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 333..369
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 371..407
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..445
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 447..482
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..520
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 522..558
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 592..624
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 626..662
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 664..700
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 702..738
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 746..777
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 779..815
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 817..853
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 860..914
FT /note="VWFC"
FT DOMAIN 918..956
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1181..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 184..193
FT /evidence="ECO:0000250"
FT DISULFID 197..209
FT /evidence="ECO:0000250"
FT DISULFID 217..226
FT /evidence="ECO:0000250"
FT DISULFID 231..242
FT /evidence="ECO:0000250"
FT DISULFID 235..248
FT /evidence="ECO:0000250"
FT DISULFID 250..259
FT /evidence="ECO:0000250"
FT DISULFID 262..273
FT /evidence="ECO:0000250"
FT DISULFID 268..279
FT /evidence="ECO:0000250"
FT DISULFID 281..290
FT /evidence="ECO:0000250"
FT DISULFID 297..309
FT /evidence="ECO:0000250"
FT DISULFID 303..319
FT /evidence="ECO:0000250"
FT DISULFID 321..330
FT /evidence="ECO:0000250"
FT DISULFID 337..348
FT /evidence="ECO:0000250"
FT DISULFID 342..357
FT /evidence="ECO:0000250"
FT DISULFID 359..368
FT /evidence="ECO:0000250"
FT DISULFID 375..386
FT /evidence="ECO:0000250"
FT DISULFID 380..395
FT /evidence="ECO:0000250"
FT DISULFID 397..406
FT /evidence="ECO:0000250"
FT DISULFID 413..424
FT /evidence="ECO:0000250"
FT DISULFID 418..433
FT /evidence="ECO:0000250"
FT DISULFID 435..444
FT /evidence="ECO:0000250"
FT DISULFID 451..461
FT /evidence="ECO:0000250"
FT DISULFID 455..470
FT /evidence="ECO:0000250"
FT DISULFID 472..481
FT /evidence="ECO:0000250"
FT DISULFID 488..499
FT /evidence="ECO:0000250"
FT DISULFID 493..508
FT /evidence="ECO:0000250"
FT DISULFID 510..519
FT /evidence="ECO:0000250"
FT DISULFID 526..537
FT /evidence="ECO:0000250"
FT DISULFID 531..546
FT /evidence="ECO:0000250"
FT DISULFID 548..557
FT /evidence="ECO:0000250"
FT DISULFID 596..612
FT /evidence="ECO:0000250"
FT DISULFID 614..623
FT /evidence="ECO:0000250"
FT DISULFID 630..641
FT /evidence="ECO:0000250"
FT DISULFID 635..650
FT /evidence="ECO:0000250"
FT DISULFID 652..661
FT /evidence="ECO:0000250"
FT DISULFID 668..679
FT /evidence="ECO:0000250"
FT DISULFID 673..688
FT /evidence="ECO:0000250"
FT DISULFID 690..699
FT /evidence="ECO:0000250"
FT DISULFID 706..717
FT /evidence="ECO:0000250"
FT DISULFID 711..726
FT /evidence="ECO:0000250"
FT DISULFID 728..737
FT /evidence="ECO:0000250"
FT DISULFID 745..756
FT /evidence="ECO:0000250"
FT DISULFID 750..765
FT /evidence="ECO:0000250"
FT DISULFID 767..776
FT /evidence="ECO:0000250"
FT DISULFID 783..794
FT /evidence="ECO:0000250"
FT DISULFID 788..803
FT /evidence="ECO:0000250"
FT DISULFID 805..814
FT /evidence="ECO:0000250"
FT DISULFID 821..832
FT /evidence="ECO:0000250"
FT DISULFID 826..841
FT /evidence="ECO:0000250"
FT DISULFID 843..852
FT /evidence="ECO:0000250"
SQ SEQUENCE 1213 AA; 133366 MW; 5C5F16A7E20D9534 CRC64;
MILRRSSVFS AFYLHAFLLC LRTTVSDASG HFELEILSMQ NANGELQNGA CCDGARNPAD
RKCTRDECDT YFKVCLKEYQ SRVSSAGACS FGTGSTPVLG GNKFSTKGTR SEKSRIVLPF
SFAWPRSYTL IVEALDFNNE TASESGKLIE KAYHSGMINP NRQWQRLTHN GPVAQFEYQI
RVTCLEHYYG FGCNKFCRPR DEFFGHYTCD QNGNKTCLEG WTGPDCNTAI CRQGCSTEHG
SCKQPGGCKC LYGWQGPYCD KCIPHPGCVH GTCVEPWQCL CDTNWGGQLC DKDLNYCGTH
QPCLNGGTCS NTGPDKYQCS CEDGYSGVNC ERAEHACLSN PCANGGTCKE TSQGYECHCA
IGWSGTSCEI NVDDCTPNQC KHGGTCQDLV NGFKCACPPH WTGKTCQIDA NECEDKPCVN
AKSCHNLIGA YFCECLPGWS GQNCDININD CKGQCLNGGT CKDLVNGYRC LCPPGYTGEQ
CEKDVDECAS SPCLNGGRCQ DEVNGFQCLC PAGFSGQLCQ LDIDYCKPNP CQNGAQCFNL
ASDYFCKCPD DYEGKNCSHL KDHCRTTSCQ VIDSCTVAVA SNSTPEGVRY ISSNVCGPHG
RCRSQAGGQF TCECQEGFRG TYCHENINDC ESNPCRNGGT CIDKVNVYQC ICADGWEGVH
CEINIDDCSL NPCLNKGACQ DLVNDFYCEC RNGWKGKTCH SRDSQCDEAT CNNGGTCHDE
GDTFKCRCSP GWEGATCNIA KNSSCLPNPC ENGGTCVVNG DSFNCVCKEG WEGSTCTENT
NDCNPHPCYN SGTCVDGENW YRCECAPGFA GPDCRININE CQSSPCAFGS TCVDEINGYR
CLCPPGRIGP DCQEVVGRPC IANGQVTADG AKWEEDCNIC QCQNGRIHCT MMWCGPKSCR
IGKARGGCPA SQSCVPIKEE QCFVKPCPSL GECWPSAPPP PSKCHASFSY QDDSCANITF
TFNKENMPQG LSVEHVCNEL RHWYLLKNLS TEYAVSISCE PSSSASNEIH ISISTEEPRT
DRSPIKDITV QIIDLVSKHN GNSTIIKAIT GVRVHQIPSP KTDYLVPLLS SIFIVLWIFA
LASAFLWCIH RRRKQNTHSN TATSATEDNT TNNVREQLNQ IKNPIEKHAA HGVPIKDYEG
KNSIIAKIRT HNSEVEEEDM DKHLQKARFT KQPAYTLVER EERAPNKNPN WTNKQDNRDL
ETAQSLNRME YIV
